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A6SUF7

- HEM1_JANMA

UniProt

A6SUF7 - HEM1_JANMA

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Protein

Glutamyl-tRNA reductase

Gene
hemA, mma_0214
Organism
Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity.UniRule annotation

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei57 – 571Nucleophile By similarity
Sitei109 – 1091Important for activity By similarity
Binding sitei119 – 1191Substrate By similarity
Binding sitei130 – 1301Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2046NADP By similarity

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciJSP375286:GJ8U-214-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:mma_0214
OrganismiJanthinobacterium sp. (strain Marseille) (Minibacterium massiliensis)
Taxonomic identifieri375286 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeJanthinobacterium
ProteomesiUP000006388: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Glutamyl-tRNA reductaseUniRule annotationPRO_0000335047Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi375286.mma_0214.

Structurei

3D structure databases

ProteinModelPortaliA6SUF7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 594Substrate binding By similarity
Regioni124 – 1263Substrate binding By similarity

Domaini

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6SUF7-1 [UniParc]FASTAAdd to Basket

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MQLLAVGLNH TTAPVSLREK VAFPADQLGQ AVASARSWYG RSDATTYTDE    50
AAILSTCNRT ELYAASNLPG GVNEAIDITA HFLADYHKLP YAELRPYLYA 100
LPQDNAVRHA FRVASGLDSM VLGEPQILGQ MKDAVRQAEA AGGLGTYLHQ 150
MFQRTFAVAK EVRSTTEIGA HSVSMAAASV RLSQRIFDKI SEQNVLFIGA 200
GEMIELSATH FAAQNPKSVT IANRTLERGQ TLAHRFNGKA IRLADLPDQL 250
ASYDIVISST ASSLPIIGLG MVERAIKARR HKPMFMVDLA VPRDIEAEIG 300
RLDDVFLYTV DDLGSFVQTG VENRQAAVAQ AEAIIETRVR SFMHWIDARA 350
VVPVIQDLHE SSETMRMIEL ERARKLLAKG EDIDAVLEAL SKGLTAKFLH 400
GPQQALNNAQ GDERARLAAL LPQLFRTKR 429
Length:429
Mass (Da):47,029
Last modified:August 21, 2007 - v1
Checksum:iB22847099D3678CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000269 Genomic DNA. Translation: ABR88801.1.
RefSeqiWP_011979440.1. NC_009659.1.
YP_001351904.1. NC_009659.1.

Genome annotation databases

EnsemblBacteriaiABR88801; ABR88801; mma_0214.
GeneIDi5351794.
KEGGimms:mma_0214.
PATRICi22152829. VBIJanSp106498_0220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000269 Genomic DNA. Translation: ABR88801.1 .
RefSeqi WP_011979440.1. NC_009659.1.
YP_001351904.1. NC_009659.1.

3D structure databases

ProteinModelPortali A6SUF7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 375286.mma_0214.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR88801 ; ABR88801 ; mma_0214 .
GeneIDi 5351794.
KEGGi mms:mma_0214.
PATRICi 22152829. VBIJanSp106498_0220.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci JSP375286:GJ8U-214-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome analysis of Minibacterium massiliensis highlights the convergent evolution of water-living bacteria."
    Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D., Drancourt M.
    PLoS Genet. 3:1454-1463(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Marseille.

Entry informationi

Entry nameiHEM1_JANMA
AccessioniPrimary (citable) accession number: A6SUF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: September 3, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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